메뉴 건너뛰기




Volumn 29, Issue , 2015, Pages 166-179

Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins

Author keywords

PCNA; Translesion synthesis; Ubiquitin; Y family polymerase

Indexed keywords

CYCLINE; DNA DIRECTED DNA POLYMERASE; LYSINE;

EID: 84939987001     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2015.02.011     Document Type: Article
Times cited : (35)

References (233)
  • 1
    • 84910679144 scopus 로고    scopus 로고
    • Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database
    • Khoury G.A., Baliban R.C., Floudas C.A. Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database. Sci. Rep. 2011, 1.
    • (2011) Sci. Rep. , vol.1
    • Khoury, G.A.1    Baliban, R.C.2    Floudas, C.A.3
  • 4
    • 84886296491 scopus 로고    scopus 로고
    • Post-translational modification of proteins in toxicological research: focus on lysine acylation
    • Lee S. Post-translational modification of proteins in toxicological research: focus on lysine acylation. Toxicol. Res. 2013, 29:81-86.
    • (2013) Toxicol. Res. , vol.29 , pp. 81-86
    • Lee, S.1
  • 6
    • 84876167149 scopus 로고    scopus 로고
    • Reading, writing, and repair: the role of ubiquitin and the ubiquitin-like proteins in DNA damage signaling and repair
    • Pinder J.B., Attwood K.M., Dellaire G. Reading, writing, and repair: the role of ubiquitin and the ubiquitin-like proteins in DNA damage signaling and repair. Front. Genet. 2013, 4.
    • (2013) Front. Genet. , vol.4
    • Pinder, J.B.1    Attwood, K.M.2    Dellaire, G.3
  • 7
    • 84903124095 scopus 로고    scopus 로고
    • Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair
    • Zhao Y., Brickner J.R., Majid M.C., Mosammaparast N. Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair. Trends Cell Biol. 2014, 24:426-434.
    • (2014) Trends Cell Biol. , vol.24 , pp. 426-434
    • Zhao, Y.1    Brickner, J.R.2    Majid, M.C.3    Mosammaparast, N.4
  • 8
    • 84877725149 scopus 로고    scopus 로고
    • Regulatory role of ubiquitin in eukaryotic DNA translesion synthesis
    • Yang K., Weinacht C.P., Zhuang Z. Regulatory role of ubiquitin in eukaryotic DNA translesion synthesis. Biochemistry 2013, 52:3217-3228.
    • (2013) Biochemistry , vol.52 , pp. 3217-3228
    • Yang, K.1    Weinacht, C.P.2    Zhuang, Z.3
  • 9
    • 84898745559 scopus 로고    scopus 로고
    • Two-way communications between ubiquitin-like modifiers and DNA
    • Ulrich H.D. Two-way communications between ubiquitin-like modifiers and DNA. Nat. Struct. Mol. Biol. 2014, 21:317-324.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 317-324
    • Ulrich, H.D.1
  • 11
    • 0037376172 scopus 로고    scopus 로고
    • Ubiquitin: not just for proteasomes anymore
    • Aguilar R.C., Wendland B. Ubiquitin: not just for proteasomes anymore. Curr. Opin. Cell Biol. 2003, 15:184-190.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 184-190
    • Aguilar, R.C.1    Wendland, B.2
  • 12
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund K., Di Fiore P.P., Dikic I. Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 2003, 28:598-603.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 13
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2001, 2:195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 14
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun L., Chen Z.J. The novel functions of ubiquitination in signaling. Curr. Opin. Cell Biol. 2004, 16:119-126.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 15
    • 84875259201 scopus 로고    scopus 로고
    • Ubiquitin-omics reveals novel networks and associations with human disease
    • Kessler B.M. Ubiquitin-omics reveals novel networks and associations with human disease. Curr. Opin. Chem. Biol. 2013, 17:59-65.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 59-65
    • Kessler, B.M.1
  • 16
    • 33748991453 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
    • Hoeller D., Hecker C.-M., Dikic I. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat. Rev. Cancer 2006, 6:776-788.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 776-788
    • Hoeller, D.1    Hecker, C.-M.2    Dikic, I.3
  • 17
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: pathogenesis of human diseases and drug targeting
    • Ciechanover A., Schwartz A.L. The ubiquitin system: pathogenesis of human diseases and drug targeting. Biochim. Biophys. Acta 2004, 1695:3-17.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 18
    • 33750946999 scopus 로고    scopus 로고
    • Narrative review: protein degradation and human diseases: the ubiquitin connection
    • Reinstein E., Ciechanover A. Narrative review: protein degradation and human diseases: the ubiquitin connection. Ann. Intern. Med. 2006, 145:676-684.
    • (2006) Ann. Intern. Med. , vol.145 , pp. 676-684
    • Reinstein, E.1    Ciechanover, A.2
  • 19
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • Petroski M.D. The ubiquitin system, disease, and drug discovery. BMC Biochem. 2008, 9(Suppl. 1):S7.
    • (2008) BMC Biochem. , vol.9 , pp. S7
    • Petroski, M.D.1
  • 20
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • Nalepa G., Rolfe M., Harper J.W. Drug discovery in the ubiquitin-proteasome system. Nat. Rev. Drug Discov. 2006, 5:596-613.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 23
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: more protein substrates join in
    • Ciechanover A., Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 2004, 14:103-106.
    • (2004) Trends Cell Biol. , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 24
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell K., Coscoy L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 2005, 309:127-130.
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 25
    • 84871995188 scopus 로고    scopus 로고
    • The lysine48-based polyubiquitin chain proteasomal signal: not a single child anymore
    • Kravtsova-Ivantsiv Y., Sommer T., Ciechanover A. The lysine48-based polyubiquitin chain proteasomal signal: not a single child anymore. Angew. Chem. Int. Ed. 2013, 52:192-198.
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 192-198
    • Kravtsova-Ivantsiv, Y.1    Sommer, T.2    Ciechanover, A.3
  • 26
    • 0026603895 scopus 로고
    • Ubiquitin-dependent protein degradation: a cellular perspective
    • Jentsch S. Ubiquitin-dependent protein degradation: a cellular perspective. Trends Cell Biol. 1992, 2:98-103.
    • (1992) Trends Cell Biol. , vol.2 , pp. 98-103
    • Jentsch, S.1
  • 27
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: on protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 1998, 17:7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 28
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 2002, 82:373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 30
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • Hofmann R.M., Pickart C.M. In vitro assembly and recognition of Lys-63 polyubiquitin chains. J. Biol. Chem. 2001, 276:27936-27943.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 31
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman R.L., Gordon C., Mayer R.J. Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat. Rev. Mol. Cell Biol. 2005, 6:599-609.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 34
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999, 96:635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 35
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H., Rape M., Braun S., Rumpf S., Hoege C., Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 2005, 120:73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 37
    • 84866913822 scopus 로고    scopus 로고
    • Modification by ubiquitin-like proteins: significance in apoptosis and autophagy pathways
    • Cajee U.-F., Hull R., Ntwasa M. Modification by ubiquitin-like proteins: significance in apoptosis and autophagy pathways. Int. J. Mol. Sci. 2012, 13:11804-11831.
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 11804-11831
    • Cajee, U.-F.1    Hull, R.2    Ntwasa, M.3
  • 38
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • Herrmann J., Lerman L.O., Lerman A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ. Res. 2007, 100:1276-1291.
    • (2007) Circ. Res. , vol.100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 39
    • 42049108221 scopus 로고    scopus 로고
    • Cell biology: SUMO
    • Meulmeester E., Melchior F. Cell biology: SUMO. Nature 2008, 452:709-711.
    • (2008) Nature , vol.452 , pp. 709-711
    • Meulmeester, E.1    Melchior, F.2
  • 40
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M. Origin and function of ubiquitin-like proteins. Nature 2009, 458:422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 41
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep. 2007, 8:550-555.
    • (2007) EMBO Rep. , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 42
    • 84888198951 scopus 로고    scopus 로고
    • SUMO rules: regulatory concepts and their implication in neurologic functions
    • Droescher M., Chaugule V.K., Pichler A. SUMO rules: regulatory concepts and their implication in neurologic functions. Neuromol. Med. 2013, 15:639-660.
    • (2013) Neuromol. Med. , vol.15 , pp. 639-660
    • Droescher, M.1    Chaugule, V.K.2    Pichler, A.3
  • 44
    • 84878579784 scopus 로고    scopus 로고
    • Sumoylation in neurodegenerative diseases
    • Krumova P., Weishaupt J.H. Sumoylation in neurodegenerative diseases. Cell. Mol. Life Sci. 2013, 70:2123-2138.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2123-2138
    • Krumova, P.1    Weishaupt, J.H.2
  • 45
    • 84858173194 scopus 로고    scopus 로고
    • SUMO downregulates GLP-1-stimulated cAMP generation and insulin secretion
    • Rajan S., Torres J., Thompson M.S., Philipson L.H. SUMO downregulates GLP-1-stimulated cAMP generation and insulin secretion. AJP Endocrinol. Metab. 2012, 302:E714-E723.
    • (2012) AJP Endocrinol. Metab. , vol.302 , pp. E714-E723
    • Rajan, S.1    Torres, J.2    Thompson, M.S.3    Philipson, L.H.4
  • 46
    • 0023160888 scopus 로고
    • Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin
    • Haas A.L., Ahrens P., Bright P.M., Ankel H. Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin. J. Biol. Chem. 1987, 262:11315-11323.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11315-11323
    • Haas, A.L.1    Ahrens, P.2    Bright, P.M.3    Ankel, H.4
  • 47
    • 33645217490 scopus 로고    scopus 로고
    • The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase
    • Zou W., Zhang D.-E. The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase. J. Biol. Chem. 2006, 281:3989-3994.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3989-3994
    • Zou, W.1    Zhang, D.-E.2
  • 48
    • 33645230779 scopus 로고    scopus 로고
    • Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells
    • Dastur A., Beaudenon S., Kelley M., Krug R.M., Huibregtse J.M. Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells. J. Biol. Chem. 2006, 281:4334-4338.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4334-4338
    • Dastur, A.1    Beaudenon, S.2    Kelley, M.3    Krug, R.M.4    Huibregtse, J.M.5
  • 50
    • 84888016188 scopus 로고    scopus 로고
    • The antiviral activities of ISG15
    • Morales D.J., Lenschow D.J. The antiviral activities of ISG15. J. Mol. Biol. 2013, 425:4995-5008.
    • (2013) J. Mol. Biol. , vol.425 , pp. 4995-5008
    • Morales, D.J.1    Lenschow, D.J.2
  • 51
    • 31544460359 scopus 로고    scopus 로고
    • Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway
    • Desai S.D. Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway. Cancer Res. 2006, 66:921-928.
    • (2006) Cancer Res. , vol.66 , pp. 921-928
    • Desai, S.D.1
  • 52
    • 0030695339 scopus 로고    scopus 로고
    • Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein
    • Kamitani T., Kito K., Nguyen H.P., Yeh E.T.H. Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein. J. Biol. Chem. 1997, 272:28557-28562.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28557-28562
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Yeh, E.T.H.4
  • 53
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes
    • Whitby F.G., Xia G., Pickart C.M., Hill C.P. Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J. Biol. Chem. 1998, 273:34983-34991.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 54
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: building an expressway to protein destruction
    • Pan Z.-Q., Kentsis A., Dias D.C., Yamoah K., Wu K. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 2004, 23:1985-1997.
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.-Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 57
    • 84901044873 scopus 로고    scopus 로고
    • Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1)-receptor Pex5p regulate PTS1 protein import
    • Okumoto K., Noda H., Fujiki Y. Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1)-receptor Pex5p regulate PTS1 protein import. J. Biol. Chem. 2014, 289:14089-14108.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14089-14108
    • Okumoto, K.1    Noda, H.2    Fujiki, Y.3
  • 58
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • Gentry M.S., Worby C.A., Dixon J.E. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:8501-8506.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 59
    • 0038128204 scopus 로고    scopus 로고
    • High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction
    • Malakhov M.P., Kim K.I., Malakhova O.A., Jacobs B.S., Borden E.C., Zhang D.-E. High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction. J. Biol. Chem. 2003, 278:16608-16613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16608-16613
    • Malakhov, M.P.1    Kim, K.I.2    Malakhova, O.A.3    Jacobs, B.S.4    Borden, E.C.5    Zhang, D.-E.6
  • 60
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111.013284
    • Wagner S.A., Beli P., Weinert B.T., Nielsen M.L., Cox J., Mann M., Choudhary C. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell. Proteomics 2011, 10. M111.013284.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.7
  • 64
    • 84885012783 scopus 로고    scopus 로고
    • Large-scale identification of ubiquitination sites by mass spectrometry
    • Udeshi N.D., Mertins P., Svinkina T., Carr S.A. Large-scale identification of ubiquitination sites by mass spectrometry. Nat. Protoc. 2013, 8:1950-1960.
    • (2013) Nat. Protoc. , vol.8 , pp. 1950-1960
    • Udeshi, N.D.1    Mertins, P.2    Svinkina, T.3    Carr, S.A.4
  • 66
  • 69
    • 54049153629 scopus 로고    scopus 로고
    • SCUD. Saccharomyces Cerevisiae Ubiquitination Database
    • Lee W.-C., Lee M., Jung J.W., Kim K.P., Kim D. SCUD. Saccharomyces Cerevisiae Ubiquitination Database. BMC Genomics 2008, 9:440.
    • (2008) BMC Genomics , vol.9 , pp. 440
    • Lee, W.-C.1    Lee, M.2    Jung, J.W.3    Kim, K.P.4    Kim, D.5
  • 70
    • 71049118572 scopus 로고    scopus 로고
    • SysPTM: a systematic resource for proteomic research on post-translational modifications
    • Li H., Xing X., Ding G., Li Q., Wang C., Xie L., Zeng R., Li Y. SysPTM: a systematic resource for proteomic research on post-translational modifications. Mol. Cell. Proteomics 2009, 8:1839-1849.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1839-1849
    • Li, H.1    Xing, X.2    Ding, G.3    Li, Q.4    Wang, C.5    Xie, L.6    Zeng, R.7    Li, Y.8
  • 73
    • 48249145694 scopus 로고    scopus 로고
    • Computational identification of ubiquitylation sites from protein sequences
    • Tung C.-W., Ho S.-Y. Computational identification of ubiquitylation sites from protein sequences. BMC Bioinform. 2008, 9:310.
    • (2008) BMC Bioinform. , vol.9 , pp. 310
    • Tung, C.-W.1    Ho, S.-Y.2
  • 75
    • 84862641013 scopus 로고    scopus 로고
    • Prediction of lysine ubiquitination with mRMR feature selection and analysis
    • Cai Y., Huang T., Hu L., Shi X., Xie L., Li Y. Prediction of lysine ubiquitination with mRMR feature selection and analysis. Amino Acids 2012, 42:1387-1395.
    • (2012) Amino Acids , vol.42 , pp. 1387-1395
    • Cai, Y.1    Huang, T.2    Hu, L.3    Shi, X.4    Xie, L.5    Li, Y.6
  • 76
    • 79960909253 scopus 로고    scopus 로고
    • Prediction of ubiquitination sites by using the composition of k-spaced amino acid pairs
    • Chen Z., Chen Y.-Z., Wang X.-F., Wang C., Yan R.-X., Zhang Z. Prediction of ubiquitination sites by using the composition of k-spaced amino acid pairs. PLoS ONE 2011, 6:e22930.
    • (2011) PLoS ONE , vol.6 , pp. e22930
    • Chen, Z.1    Chen, Y.-Z.2    Wang, X.-F.3    Wang, C.4    Yan, R.-X.5    Zhang, Z.6
  • 77
    • 84882262248 scopus 로고    scopus 로고
    • HCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties
    • Chen Z., Zhou Y., Song J., Zhang Z. hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Biochim. Biophys. Acta 2013, 1834:1461-1467.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1461-1467
    • Chen, Z.1    Zhou, Y.2    Song, J.3    Zhang, Z.4
  • 78
    • 84898906108 scopus 로고    scopus 로고
    • RUBI: rapid proteomic-scale prediction of lysine ubiquitination and factors influencing predictor performance
    • Walsh I., Di Domenico T., Tosatto S.C.E. RUBI: rapid proteomic-scale prediction of lysine ubiquitination and factors influencing predictor performance. Amino Acids 2014, 46:853-862.
    • (2014) Amino Acids , vol.46 , pp. 853-862
    • Walsh, I.1    Di Domenico, T.2    Tosatto, S.C.E.3
  • 79
    • 84879895159 scopus 로고    scopus 로고
    • Incorporating key position and amino acid residue features to identify general and species-specific ubiquitin conjugation sites
    • Chen X., Qiu J.-D., Shi S.-P., Suo S.-B., Huang S.-Y., Liang R.-P. Incorporating key position and amino acid residue features to identify general and species-specific ubiquitin conjugation sites. Bioinformatics (Oxf., Engl.) 2013, 29:1614-1622.
    • (2013) Bioinformatics (Oxf., Engl.) , vol.29 , pp. 1614-1622
    • Chen, X.1    Qiu, J.-D.2    Shi, S.-P.3    Suo, S.-B.4    Huang, S.-Y.5    Liang, R.-P.6
  • 80
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson D.A., Wang M., Matunis M.J. The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 2001, 276:21664-21669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 82
    • 23144452431 scopus 로고    scopus 로고
    • GPS: a comprehensive www server for phosphorylation sites prediction
    • Xue Y., Zhou F., Zhu M., Ahmed K., Chen G., Yao X. GPS: a comprehensive www server for phosphorylation sites prediction. Nucleic Acids Res. 2005, 33:W184-W187.
    • (2005) Nucleic Acids Res. , vol.33 , pp. W184-W187
    • Xue, Y.1    Zhou, F.2    Zhu, M.3    Ahmed, K.4    Chen, G.5    Yao, X.6
  • 83
    • 33747838835 scopus 로고    scopus 로고
    • SUMOsp: a web server for sumoylation site prediction
    • Xue Y., Zhou F., Fu C., Xu Y., Yao X. SUMOsp: a web server for sumoylation site prediction. Nucleic Acids Res. 2006, 34:W254-W257.
    • (2006) Nucleic Acids Res. , vol.34 , pp. W254-W257
    • Xue, Y.1    Zhou, F.2    Fu, C.3    Xu, Y.4    Yao, X.5
  • 84
    • 8844284560 scopus 로고    scopus 로고
    • GPS: a novel group-based phosphorylation predicting and scoring method
    • Zhou F.-F., Xue Y., Chen G.-L., Yao X. GPS: a novel group-based phosphorylation predicting and scoring method. Biochem. Biophys. Res. Commun. 2004, 325:1443-1448.
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 1443-1448
    • Zhou, F.-F.1    Xue, Y.2    Chen, G.-L.3    Yao, X.4
  • 85
    • 8844219516 scopus 로고    scopus 로고
    • Prediction of phosphorylation sites using SVMs
    • Kim J.H., Lee J., Oh B., Kimm K., Koh I. Prediction of phosphorylation sites using SVMs. Bioinformatics 2004, 20:3179-3184.
    • (2004) Bioinformatics , vol.20 , pp. 3179-3184
    • Kim, J.H.1    Lee, J.2    Oh, B.3    Kimm, K.4    Koh, I.5
  • 86
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0
    • Ren J., Gao X., Jin C., Zhu M., Wang X., Shaw A., Wen L., Yao X., Xue Y. Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0. Proteomics 2009, 9:3409-3412.
    • (2009) Proteomics , vol.9 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3    Zhu, M.4    Wang, X.5    Shaw, A.6    Wen, L.7    Yao, X.8    Xue, Y.9
  • 87
    • 84862758300 scopus 로고    scopus 로고
    • Predicting protein sumoylation sites from sequence features
    • Teng S., Luo H., Wang L. Predicting protein sumoylation sites from sequence features. Amino Acids 2012, 43:447-455.
    • (2012) Amino Acids , vol.43 , pp. 447-455
    • Teng, S.1    Luo, H.2    Wang, L.3
  • 88
    • 84867623385 scopus 로고    scopus 로고
    • Prediction of lysine post-translational modifications using bioinformatic tools
    • Schwartz D. Prediction of lysine post-translational modifications using bioinformatic tools. Essays Biochem. 2012, 52:165-177.
    • (2012) Essays Biochem. , vol.52 , pp. 165-177
    • Schwartz, D.1
  • 91
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer D., Wang X., Huang L., Kaiser P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J. Proteome Res. 2008, 7:4566-4576.
    • (2008) J. Proteome Res. , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 93
    • 84922587024 scopus 로고    scopus 로고
    • Profiling lysine ubiquitination by selective enrichment of ubiquitin remnant-containing peptides
    • Xu G., Deglincerti A., Paige J.S., Jaffrey S.R. Profiling lysine ubiquitination by selective enrichment of ubiquitin remnant-containing peptides. Methods Mol. Biol. (Clifton, NJ) 2014, 1174:57-71.
    • (2014) Methods Mol. Biol. (Clifton, NJ) , vol.1174 , pp. 57-71
    • Xu, G.1    Deglincerti, A.2    Paige, J.S.3    Jaffrey, S.R.4
  • 94
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal A.C.O., Andersen J.S., Ogg S.C., Hay R.T., Mann M., Lamond A.I. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell. Proteomics 2006, 12:2298-2310.
    • (2006) Mol. Cell. Proteomics , vol.12 , pp. 2298-2310
    • Vertegaal, A.C.O.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 98
    • 34147173417 scopus 로고    scopus 로고
    • On the proper use of mass accuracy in proteomics
    • Zubarev R., Mann M. On the proper use of mass accuracy in proteomics. Mol. Cell. Proteomics 2007, 6:377-381.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 377-381
    • Zubarev, R.1    Mann, M.2
  • 100
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome
    • Peng J., Elias J.E., Thoreen C.C., Licklider L.J., Gygi S.P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2:43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 101
    • 79955780605 scopus 로고    scopus 로고
    • A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development
    • M110.002188
    • Franco M., Seyfried N.T., Brand A.H., Peng J., Mayor U. A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development. Mol. Cell. Proteomics 2011, 10. M110.002188.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Franco, M.1    Seyfried, N.T.2    Brand, A.H.3    Peng, J.4    Mayor, U.5
  • 102
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu G., Paige J.S., Jaffrey S.R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 2010, 28:868-873.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 105
    • 79955776357 scopus 로고    scopus 로고
    • Ubiquitinated proteome: ready for global?
    • R110.006882
    • Shi Y., Xu P., Qin J. Ubiquitinated proteome: ready for global?. Mol. Cell. Proteomics 2011, 10. R110.006882.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Shi, Y.1    Xu, P.2    Qin, J.3
  • 106
    • 84863507629 scopus 로고    scopus 로고
    • NEDD8 overexpression results in neddylation of ubiquitin substrates by the ubiquitin pathway
    • Hjerpe R., Thomas Y., Kurz T. NEDD8 overexpression results in neddylation of ubiquitin substrates by the ubiquitin pathway. J. Mol. Biol. 2012, 421:27-29.
    • (2012) J. Mol. Biol. , vol.421 , pp. 27-29
    • Hjerpe, R.1    Thomas, Y.2    Kurz, T.3
  • 114
    • 2442703973 scopus 로고    scopus 로고
    • Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins
    • Zhao Y., Kwon S.W., Anselmo A., Kaur K., White M.A. Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. J. Biol. Chem. 2004, 279:20999-21002.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20999-21002
    • Zhao, Y.1    Kwon, S.W.2    Anselmo, A.3    Kaur, K.4    White, M.A.5
  • 115
    • 84888197763 scopus 로고    scopus 로고
    • Proteomics strategies to identify SUMO targets and acceptor sites: a survey of RNA-binding proteins SUMOylation
    • Filosa G., Barabino S.M.L., Bachi A. Proteomics strategies to identify SUMO targets and acceptor sites: a survey of RNA-binding proteins SUMOylation. Neuromol. Med. 2013, 15:661-676.
    • (2013) Neuromol. Med. , vol.15 , pp. 661-676
    • Filosa, G.1    Barabino, S.M.L.2    Bachi, A.3
  • 116
    • 39649100680 scopus 로고    scopus 로고
    • Ubiquitin proteolytic system: focus on SUMO
    • Wilson V.G., Heaton P.R. Ubiquitin proteolytic system: focus on SUMO. Expert Rev. Proteomics 2008, 5:121-135.
    • (2008) Expert Rev. Proteomics , vol.5 , pp. 121-135
    • Wilson, V.G.1    Heaton, P.R.2
  • 117
    • 84871272921 scopus 로고    scopus 로고
    • A novel approach to the analysis of SUMOylation with the independent use of trypsin and elastase digestion followed by database searching utilising consecutive residue addition to lysine
    • Chicooree N., Griffiths J.R., Connolly Y., Tan C.-T., Malliri A., Eyers C.E., Smith D.L. A novel approach to the analysis of SUMOylation with the independent use of trypsin and elastase digestion followed by database searching utilising consecutive residue addition to lysine. Rapid Commun. Mass Spectrom. 2013, 27:127-134.
    • (2013) Rapid Commun. Mass Spectrom. , vol.27 , pp. 127-134
    • Chicooree, N.1    Griffiths, J.R.2    Connolly, Y.3    Tan, C.-T.4    Malliri, A.5    Eyers, C.E.6    Smith, D.L.7
  • 118
    • 44449129585 scopus 로고    scopus 로고
    • A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins
    • Jones J., Wu K., Yang Y., Guerrero C., Nillegoda N., Pan Z.-Q., Huang L. A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins. J. Proteome Res. 2008, 7:1274-1287.
    • (2008) J. Proteome Res. , vol.7 , pp. 1274-1287
    • Jones, J.1    Wu, K.2    Yang, Y.3    Guerrero, C.4    Nillegoda, N.5    Pan, Z.-Q.6    Huang, L.7
  • 119
    • 22544487172 scopus 로고    scopus 로고
    • Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways
    • Zhao C., Denison C., Huibregtse J.M., Gygi S., Krug R.M. Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:10200-10205.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10200-10205
    • Zhao, C.1    Denison, C.2    Huibregtse, J.M.3    Gygi, S.4    Krug, R.M.5
  • 120
    • 29544437558 scopus 로고    scopus 로고
    • Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions
    • Lopes M., Foiani M., Sogo J.M. Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions. Mol. Cell 2006, 21:15-27.
    • (2006) Mol. Cell , vol.21 , pp. 15-27
    • Lopes, M.1    Foiani, M.2    Sogo, J.M.3
  • 121
    • 80052768689 scopus 로고    scopus 로고
    • Ubiquitin family modifications and template switching
    • Branzei D. Ubiquitin family modifications and template switching. FEBS Lett. 2011, 585:2810-2817.
    • (2011) FEBS Lett. , vol.585 , pp. 2810-2817
    • Branzei, D.1
  • 122
    • 0033899540 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways
    • Xiao W., Chow B.L., Broomfield S., Hanna M. The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways. Genetics 2000, 155:1633-1641.
    • (2000) Genetics , vol.155 , pp. 1633-1641
    • Xiao, W.1    Chow, B.L.2    Broomfield, S.3    Hanna, M.4
  • 123
    • 0035833662 scopus 로고    scopus 로고
    • DNA postreplication repair and mutagenesis in Saccharomyces cerevisiae
    • Broomfield S., Hryciw T., Xiao W. DNA postreplication repair and mutagenesis in Saccharomyces cerevisiae. Mutat. Res. 2001, 486:167-184.
    • (2001) Mutat. Res. , vol.486 , pp. 167-184
    • Broomfield, S.1    Hryciw, T.2    Xiao, W.3
  • 124
    • 0035946012 scopus 로고    scopus 로고
    • Evolution of the two-step model for UV-mutagenesis
    • Woodgate R. Evolution of the two-step model for UV-mutagenesis. Mutat. Res. 2001, 485:83-92.
    • (2001) Mutat. Res. , vol.485 , pp. 83-92
    • Woodgate, R.1
  • 125
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 1994, 79:1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 126
    • 80052713687 scopus 로고    scopus 로고
    • Ub-family modifications at the replication fork: regulating PCNA-interacting components
    • Kirchmaier A.L. Ub-family modifications at the replication fork: regulating PCNA-interacting components. FEBS Lett. 2011, 585:2920-2928.
    • (2011) FEBS Lett. , vol.585 , pp. 2920-2928
    • Kirchmaier, A.L.1
  • 128
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan G.-L., Pfander B., Jentsch S. PCNA, the maestro of the replication fork. Cell 2007, 129:665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.-L.1    Pfander, B.2    Jentsch, S.3
  • 129
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002, 419:135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 130
    • 71349084952 scopus 로고    scopus 로고
    • Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5
    • Parker J.L., Ulrich H.D. Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5. EMBO J. 2009, 28:3657-3666.
    • (2009) EMBO J. , vol.28 , pp. 3657-3666
    • Parker, J.L.1    Ulrich, H.D.2
  • 133
    • 70349329465 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Rad6 postreplication repair and Siz1/Srs2 homologous recombination-inhibiting pathways process DNA damage that arises in asf1 mutants
    • Kats E.S., Enserink J.M., Martinez S., Kolodner R.D. The Saccharomyces cerevisiae Rad6 postreplication repair and Siz1/Srs2 homologous recombination-inhibiting pathways process DNA damage that arises in asf1 mutants. Mol. Cell. Biol. 2009, 29:5226-5237.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5226-5237
    • Kats, E.S.1    Enserink, J.M.2    Martinez, S.3    Kolodner, R.D.4
  • 134
    • 73649125005 scopus 로고    scopus 로고
    • CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis
    • Terai K., Abbas T., Jazaeri A.A., Dutta A. CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis. Mol. Cell 2010, 37:143-149.
    • (2010) Mol. Cell , vol.37 , pp. 143-149
    • Terai, K.1    Abbas, T.2    Jazaeri, A.A.3    Dutta, A.4
  • 139
    • 84864378326 scopus 로고    scopus 로고
    • Epstein-Barr virus BPLF1 deubiquitinates PCNA and attenuates polymerase η recruitment to DNA damage sites
    • Whitehurst C.B., Vaziri C., Shackelford J., Pagano J.S. Epstein-Barr virus BPLF1 deubiquitinates PCNA and attenuates polymerase η recruitment to DNA damage sites. J. Virol. 2012, 86:8097-8106.
    • (2012) J. Virol. , vol.86 , pp. 8097-8106
    • Whitehurst, C.B.1    Vaziri, C.2    Shackelford, J.3    Pagano, J.S.4
  • 140
    • 33845310025 scopus 로고    scopus 로고
    • Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination
    • Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K. Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination. J. Cell Biol. 2006, 175:703-708.
    • (2006) J. Cell Biol. , vol.175 , pp. 703-708
    • Motegi, A.1    Sood, R.2    Moinova, H.3    Markowitz, S.D.4    Liu, P.P.5    Myung, K.6
  • 143
    • 41649083002 scopus 로고    scopus 로고
    • Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination
    • Unk I., Hajdú I., Fátyol K., Hurwitz J., Yoon J., Prakash L., Prakash S., Haracska L. Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination. PNAS 2008, 105:3768-3773.
    • (2008) PNAS , vol.105 , pp. 3768-3773
    • Unk, I.1    Hajdú, I.2    Fátyol, K.3    Hurwitz, J.4    Yoon, J.5    Prakash, L.6    Prakash, S.7    Haracska, L.8
  • 144
    • 79954505570 scopus 로고    scopus 로고
    • SHPRH and HLTF act in a damage-specific manner to coordinate different forms of postreplication repair and prevent mutagenesis
    • Lin J.-R., Zeman M.K., Chen J.-Y., Yee M.-C., Cimprich K.A. SHPRH and HLTF act in a damage-specific manner to coordinate different forms of postreplication repair and prevent mutagenesis. Mol. Cell 2011, 48:237-249.
    • (2011) Mol. Cell , vol.48 , pp. 237-249
    • Lin, J.-R.1    Zeman, M.K.2    Chen, J.-Y.3    Yee, M.-C.4    Cimprich, K.A.5
  • 148
    • 77955904679 scopus 로고    scopus 로고
    • A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA
    • Groehler A.L., Lannigan D.A. A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA. J. Cell Biol. 2010, 190:575-586.
    • (2010) J. Cell Biol. , vol.190 , pp. 575-586
    • Groehler, A.L.1    Lannigan, D.A.2
  • 149
    • 84904018869 scopus 로고    scopus 로고
    • NRAGE promotes cell proliferation by stabilizing PCNA in a ubiquitin-proteasome pathway in esophageal carcinomas
    • Yang Q., Ou C., Liu M., Xiao W., Wen C., Sun F. NRAGE promotes cell proliferation by stabilizing PCNA in a ubiquitin-proteasome pathway in esophageal carcinomas. Carcinogenesis 2014, 35:1643-1651.
    • (2014) Carcinogenesis , vol.35 , pp. 1643-1651
    • Yang, Q.1    Ou, C.2    Liu, M.3    Xiao, W.4    Wen, C.5    Sun, F.6
  • 151
    • 29144501653 scopus 로고    scopus 로고
    • Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts
    • Leach C.A., Michael W.M. Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts. J. Cell Biol. 2005, 171:947-954.
    • (2005) J. Cell Biol. , vol.171 , pp. 947-954
    • Leach, C.A.1    Michael, W.M.2
  • 154
    • 0037225962 scopus 로고    scopus 로고
    • Unconventional tethering of Ulp1 to the transport channel of the nuclear pore complex by karyopherins
    • Panse V.G., Küster B., Gerstberger T., Hurt E. Unconventional tethering of Ulp1 to the transport channel of the nuclear pore complex by karyopherins. Nat. Cell Biol. 2003, 5:21-27.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 21-27
    • Panse, V.G.1    Küster, B.2    Gerstberger, T.3    Hurt, E.4
  • 155
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E., Chen S., Davies A.A., Huttner D., Krejci L., Sung P., Ulrich H.D. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell 2005, 19:123-133.
    • (2005) Mol. Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 157
    • 84876837172 scopus 로고    scopus 로고
    • The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication
    • Kubota T., Nishimura K., Kanemaki M.T., Donaldson A.D. The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication. Mol. Cell 2013, 50:273-280.
    • (2013) Mol. Cell , vol.50 , pp. 273-280
    • Kubota, T.1    Nishimura, K.2    Kanemaki, M.T.3    Donaldson, A.D.4
  • 159
    • 77951210668 scopus 로고    scopus 로고
    • Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1
    • Lee K.Y., Yang K., Cohn M.A., Sikdar N., D'Andrea A.D., Myung K. Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1. J. Biol. Chem. 2010, 285:10362-10369.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10362-10369
    • Lee, K.Y.1    Yang, K.2    Cohn, M.A.3    Sikdar, N.4    D'Andrea, A.D.5    Myung, K.6
  • 160
    • 84872087979 scopus 로고    scopus 로고
    • ATAD5 regulates the lifespan of DNA replication factories by modulating PCNA level on the chromatin
    • Lee K.Y., Fu H., Aladjem M.I., Myung K. ATAD5 regulates the lifespan of DNA replication factories by modulating PCNA level on the chromatin. J. Cell Biol. 2013, 200:31-44.
    • (2013) J. Cell Biol. , vol.200 , pp. 31-44
    • Lee, K.Y.1    Fu, H.2    Aladjem, M.I.3    Myung, K.4
  • 161
    • 72449183211 scopus 로고    scopus 로고
    • Establishment of sister chromatid cohesion
    • Skibbens R.V. Establishment of sister chromatid cohesion. Curr. Biol. 2009, 19:R1126-R1132.
    • (2009) Curr. Biol. , vol.19 , pp. R1126-R1132
    • Skibbens, R.V.1
  • 162
    • 84901228683 scopus 로고    scopus 로고
    • Modification of PCNA by ISG15 plays a crucial role in termination of error-prone translesion DNA synthesis
    • Park J.M., Yang S.W., Yu K.R., Ka S.H., Lee S.W., Seol J.H., Jeon Y.J., Chung C.H. Modification of PCNA by ISG15 plays a crucial role in termination of error-prone translesion DNA synthesis. Mol. Cell 2014, 54:626-638.
    • (2014) Mol. Cell , vol.54 , pp. 626-638
    • Park, J.M.1    Yang, S.W.2    Yu, K.R.3    Ka, S.H.4    Lee, S.W.5    Seol, J.H.6    Jeon, Y.J.7    Chung, C.H.8
  • 163
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability
    • Caron C., Boyault C., Khochbin S. Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability. BioEssays News Rev. Mol. Cell. Dev. Biol. 2005, 27 4:408-415.
    • (2005) BioEssays News Rev. Mol. Cell. Dev. Biol. , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 164
    • 2442431498 scopus 로고    scopus 로고
    • The post-translational modifications of proliferating cell nuclear antigen: acetylation, not phosphorylation, plays an important role in the regulation of its function
    • Naryzhny S.N., Lee H. The post-translational modifications of proliferating cell nuclear antigen: acetylation, not phosphorylation, plays an important role in the regulation of its function. J. Biol. Chem. 2004, 279:20194-20199.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20194-20199
    • Naryzhny, S.N.1    Lee, H.2
  • 165
    • 84861858876 scopus 로고    scopus 로고
    • Structure of monoubiquitinated PCNA: implications for DNA polymerase switching and Okazaki fragment maturation
    • Zhang Z., Zhang S., Lin S.H.S., Wang X., Wu L., Lee E.Y.C., Lee M.Y.W.T. Structure of monoubiquitinated PCNA: implications for DNA polymerase switching and Okazaki fragment maturation. Cell Cycle (Georgetown, Tex.) 2012, 11:2128-2136.
    • (2012) Cell Cycle (Georgetown, Tex.) , vol.11 , pp. 2128-2136
    • Zhang, Z.1    Zhang, S.2    Lin, S.H.S.3    Wang, X.4    Wu, L.5    Lee, E.Y.C.6    Lee, M.Y.W.T.7
  • 166
    • 58149352656 scopus 로고    scopus 로고
    • Lys-110 is essential for targeting PCNA to replication and repair foci, and the K110A mutant activates apoptosis
    • Kim B.J., Lee H. Lys-110 is essential for targeting PCNA to replication and repair foci, and the K110A mutant activates apoptosis. Biol. Cell 2008, 100:675-686.
    • (2008) Biol. Cell , vol.100 , pp. 675-686
    • Kim, B.J.1    Lee, H.2
  • 170
    • 75949107942 scopus 로고    scopus 로고
    • Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y Family DNA polymerases ι and Rev1
    • Bomar M.G., D'Souza S., Bienko M., Dikic I., Walker G.C., Zhou P. Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y Family DNA polymerases ι and Rev1. Mol. Cell 2010, 37:408-417.
    • (2010) Mol. Cell , vol.37 , pp. 408-417
    • Bomar, M.G.1    D'Souza, S.2    Bienko, M.3    Dikic, I.4    Walker, G.C.5    Zhou, P.6
  • 172
    • 33846640580 scopus 로고    scopus 로고
    • Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae
    • Skoneczna A., McIntyre J., Skoneczny M., Policinska Z., Sledziewska-Gojska E. Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae. J. Mol. Biol. 2007, 366:1074-1086.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1074-1086
    • Skoneczna, A.1    McIntyre, J.2    Skoneczny, M.3    Policinska, Z.4    Sledziewska-Gojska, E.5
  • 173
    • 38849205431 scopus 로고    scopus 로고
    • Regulation of Saccharomyces cerevisiae DNA polymerase η transcript and protein
    • Pabla R., Rozario D., Siede W. Regulation of Saccharomyces cerevisiae DNA polymerase η transcript and protein. Radiat. Environ. Biophys. 2008, 47:157-168.
    • (2008) Radiat. Environ. Biophys. , vol.47 , pp. 157-168
    • Pabla, R.1    Rozario, D.2    Siede, W.3
  • 174
    • 57749101303 scopus 로고    scopus 로고
    • Regulated proteolysis of DNA polymerase eta during the DNA damage response in C. elegans
    • Kim S.-H., Michael W.M. Regulated proteolysis of DNA polymerase eta during the DNA damage response in C. elegans. Mol. Cell 2008, 32:757-766.
    • (2008) Mol. Cell , vol.32 , pp. 757-766
    • Kim, S.-H.1    Michael, W.M.2
  • 175
    • 33847381960 scopus 로고    scopus 로고
    • Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase η in Saccharomyces cerevisiae
    • Parker J.L., Bielen A.B., Dikic I., Ulrich H.D. Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase η in Saccharomyces cerevisiae. Nucleic Acids Res. 2007, 35:881-889.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 881-889
    • Parker, J.L.1    Bielen, A.B.2    Dikic, I.3    Ulrich, H.D.4
  • 177
    • 41949130152 scopus 로고    scopus 로고
    • Requirements for the interaction of mouse Polκ with ubiquitin and its biological significance
    • Guo C., Tang T.S., Bienko M., Dikic I., Friedberg E.C. Requirements for the interaction of mouse Polκ with ubiquitin and its biological significance. J. Biol. Chem. 2008, 283:4658-4664.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4658-4664
    • Guo, C.1    Tang, T.S.2    Bienko, M.3    Dikic, I.4    Friedberg, E.C.5
  • 180
    • 33750529154 scopus 로고    scopus 로고
    • Working out coupled monoubiquitination
    • Haglund K., Stenmark H. Working out coupled monoubiquitination. Nat. Cell Biol. 2006, 8:1218-1219.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1218-1219
    • Haglund, K.1    Stenmark, H.2
  • 181
    • 84864057454 scopus 로고    scopus 로고
    • A Broad requirement for TLS polymerases η and κ, and interacting sumoylation and nuclear pore proteins, in lesion bypass during C. elegans embryogenesis
    • Roerink S.F., Koole W., Stapel L.C., Romeijn R.J., Tijsterman M. A Broad requirement for TLS polymerases η and κ, and interacting sumoylation and nuclear pore proteins, in lesion bypass during C. elegans embryogenesis. PLoS Genet. 2012, 8:e1002800.
    • (2012) PLoS Genet. , vol.8 , pp. e1002800
    • Roerink, S.F.1    Koole, W.2    Stapel, L.C.3    Romeijn, R.J.4    Tijsterman, M.5
  • 184
    • 75749108557 scopus 로고    scopus 로고
    • Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation
    • Jung Y.-S., Liu G., Chen X. Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation. Mol. Cell. Biol. 2010, 30:1041-1048.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1041-1048
    • Jung, Y.-S.1    Liu, G.2    Chen, X.3
  • 185
    • 80053579178 scopus 로고    scopus 로고
    • Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis
    • Jung Y.-S., Hakem A., Hakem R., Chen X. Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis. Mol. Cell. Biol. 2011, 31:3997-4006.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3997-4006
    • Jung, Y.-S.1    Hakem, A.2    Hakem, R.3    Chen, X.4
  • 186
    • 84855850825 scopus 로고    scopus 로고
    • DNA polymerase eta is targeted by Mdm2 for polyubiquitination and proteasomal degradation in response to ultraviolet irradiation
    • Jung Y.-S., Qian Y., Chen X. DNA polymerase eta is targeted by Mdm2 for polyubiquitination and proteasomal degradation in response to ultraviolet irradiation. DNA Repair 2012, 11:177-184.
    • (2012) DNA Repair , vol.11 , pp. 177-184
    • Jung, Y.-S.1    Qian, Y.2    Chen, X.3
  • 189
    • 84940961729 scopus 로고    scopus 로고
    • USP7 modulates UV-induced PCNA monoubiquitination by regulating DNA polymerase eta stability
    • [Epub ahead of print]
    • Qian J., Pentz K., Zhu Q., Wang Q., He J., Srivastava A.K., Wani A.A. USP7 modulates UV-induced PCNA monoubiquitination by regulating DNA polymerase eta stability. Oncogene 2014, [Epub ahead of print].
    • (2014) Oncogene
    • Qian, J.1    Pentz, K.2    Zhu, Q.3    Wang, Q.4    He, J.5    Srivastava, A.K.6    Wani, A.A.7
  • 190
    • 84939996883 scopus 로고    scopus 로고
    • The steady-state level and stability of TLS polymerase eta are cell cycle dependent in the yeast S. cerevisiae
    • Plachta M., Halas A., McIntyre J., Sledziewska-Gojska E. The steady-state level and stability of TLS polymerase eta are cell cycle dependent in the yeast S. cerevisiae. DNA Repair 2015, 29:147-153.
    • (2015) DNA Repair , vol.29 , pp. 147-153
    • Plachta, M.1    Halas, A.2    McIntyre, J.3    Sledziewska-Gojska, E.4
  • 192
    • 78951472910 scopus 로고    scopus 로고
    • ATR-mediated phosphorylation of DNA polymerase η is needed for efficient recovery from UV damage
    • Gohler T., Sabbioneda S., Green C.M., Lehmann A.R. ATR-mediated phosphorylation of DNA polymerase η is needed for efficient recovery from UV damage. J. Cell Biol. 2011, 192:219-227.
    • (2011) J. Cell Biol. , vol.192 , pp. 219-227
    • Gohler, T.1    Sabbioneda, S.2    Green, C.M.3    Lehmann, A.R.4
  • 194
    • 34248195087 scopus 로고    scopus 로고
    • Evidence that in xeroderma pigmentosum variant cells, which lack DNA polymerase η, DNA polymerase ι causes the very high frequency and unique spectrum of UV-induced mutations
    • Wang Y., Woodgate R., McManus T.P., Mead S., McCormick J.J., Maher V.M. Evidence that in xeroderma pigmentosum variant cells, which lack DNA polymerase η, DNA polymerase ι causes the very high frequency and unique spectrum of UV-induced mutations. Cancer Res. 2007, 67:3018-3026.
    • (2007) Cancer Res. , vol.67 , pp. 3018-3026
    • Wang, Y.1    Woodgate, R.2    McManus, T.P.3    Mead, S.4    McCormick, J.J.5    Maher, V.M.6
  • 197
    • 67650928194 scopus 로고    scopus 로고
    • DNA polymerase ζ cooperates with polymerases κ and ι in translesion DNA synthesis across pyrimidine photodimers in cells from XPV patients
    • Ziv O., Geacintov N., Nakajima S., Yasui A., Livneh Z. DNA polymerase ζ cooperates with polymerases κ and ι in translesion DNA synthesis across pyrimidine photodimers in cells from XPV patients. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:11552-11557.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11552-11557
    • Ziv, O.1    Geacintov, N.2    Nakajima, S.3    Yasui, A.4    Livneh, Z.5
  • 198
    • 84922513826 scopus 로고    scopus 로고
    • Redundancy of mammalian Y family DNA polymerases in cellular responses to genomic DNA lesions induced by ultraviolet light
    • Jansen J.G., Temviriyanukul P., Wit N., Delbos F., Reynaud C.-A., Jacobs H., de Wind N. Redundancy of mammalian Y family DNA polymerases in cellular responses to genomic DNA lesions induced by ultraviolet light. Nucleic Acids Res. 2014, 42:11071-11082.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 11071-11082
    • Jansen, J.G.1    Temviriyanukul, P.2    Wit, N.3    Delbos, F.4    Reynaud, C.-A.5    Jacobs, H.6    de Wind, N.7
  • 199
    • 34548337284 scopus 로고    scopus 로고
    • Increased catalytic activity and altered fidelity of human DNA polymerase ι in the presence of manganese
    • Frank E.G., Woodgate R. Increased catalytic activity and altered fidelity of human DNA polymerase ι in the presence of manganese. J. Biol. Chem. 2007, 282:24689-24696.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24689-24696
    • Frank, E.G.1    Woodgate, R.2
  • 200
    • 0034596992 scopus 로고    scopus 로고
    • Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase ι
    • Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R. Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase ι. EMBO J. 2000, 19:5259-5266.
    • (2000) EMBO J. , vol.19 , pp. 5259-5266
    • Tissier, A.1    Frank, E.G.2    McDonald, J.P.3    Iwai, S.4    Hanaoka, F.5    Woodgate, R.6
  • 202
  • 205
    • 0033830464 scopus 로고    scopus 로고
    • Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι
    • Zhang Y., Yuan F., Wu X., Wang Z. Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι. Mol. Cell. Biol. 2000, 20:7099-7108.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7099-7108
    • Zhang, Y.1    Yuan, F.2    Wu, X.3    Wang, Z.4
  • 206
    • 79952763415 scopus 로고    scopus 로고
    • Unique active site promotes error-free replication opposite an 8-oxo-guanine lesion by human DNA polymerase iota
    • Kirouac K.N., Ling H. Unique active site promotes error-free replication opposite an 8-oxo-guanine lesion by human DNA polymerase iota. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:3210-3215.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3210-3215
    • Kirouac, K.N.1    Ling, H.2
  • 207
    • 26444528004 scopus 로고    scopus 로고
    • Human DNA polymerase ι incorporates dCTP opposite template G via a G.C.+Hoogsteen base pair
    • Nair D.T., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K. Human DNA polymerase ι incorporates dCTP opposite template G via a G.C.+Hoogsteen base pair. Structure 2005, 13:1569-1577.
    • (2005) Structure , vol.13 , pp. 1569-1577
    • Nair, D.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4    Aggarwal, A.K.5
  • 209
    • 0042031052 scopus 로고    scopus 로고
    • Localization of the deoxyribose phosphate lyase active site in human DNA polymerase ι by controlled proteolysis
    • Prasad R., Bebenek K., Hou E., Shock D.D., Beard W.A., Woodgate R., Kunkel T.A., Wilson S.H. Localization of the deoxyribose phosphate lyase active site in human DNA polymerase ι by controlled proteolysis. J. Biol. Chem. 2003, 278:29649-29654.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29649-29654
    • Prasad, R.1    Bebenek, K.2    Hou, E.3    Shock, D.D.4    Beard, W.A.5    Woodgate, R.6    Kunkel, T.A.7    Wilson, S.H.8
  • 213
    • 0037133339 scopus 로고    scopus 로고
    • Human DINB1-encoded DNA polymerase κ is a promiscuous extender of mispaired primer termini
    • Washington M.T., Johnson R.E., Prakash L., Prakash S. Human DINB1-encoded DNA polymerase κ is a promiscuous extender of mispaired primer termini. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:1910-1914.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1910-1914
    • Washington, M.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 214
    • 33744789415 scopus 로고    scopus 로고
    • The Y-family DNA polymerase κ (pol κ) functions in mammalian nucleotide-excision repair
    • Ogi T., Lehmann A.R. The Y-family DNA polymerase κ (pol κ) functions in mammalian nucleotide-excision repair. Nat. Cell Biol. 2006, 8:640-642.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 640-642
    • Ogi, T.1    Lehmann, A.R.2
  • 215
    • 84857411787 scopus 로고    scopus 로고
    • Y-family DNA polymerases and their role in tolerance of cellular DNA damage
    • Sale J.E., Lehmann A.R., Woodgate R. Y-family DNA polymerases and their role in tolerance of cellular DNA damage. Nat. Rev. Mol. Cell Biol. 2012, 13:141-152.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 141-152
    • Sale, J.E.1    Lehmann, A.R.2    Woodgate, R.3
  • 218
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 1996, 382:729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 220
    • 0033571521 scopus 로고    scopus 로고
    • The human REV1 gene codes for a DNA template-dependent dCMP transferase
    • Lin W., Xin H., Zhang Y., Wu X., Yuan F., Wang Z. The human REV1 gene codes for a DNA template-dependent dCMP transferase. Nucleic Acids Res. 1999, 27:4468-4475.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4468-4475
    • Lin, W.1    Xin, H.2    Zhang, Y.3    Wu, X.4    Yuan, F.5    Wang, Z.6
  • 221
    • 0036529562 scopus 로고    scopus 로고
    • Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion
    • Zhang Y. Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion. Nucleic Acids Res. 2002, 30:1630-1638.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1630-1638
    • Zhang, Y.1
  • 222
    • 14844362615 scopus 로고    scopus 로고
    • Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1
    • Ross A.-L. Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1. Nucleic Acids Res. 2005, 33:1280-1289.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1280-1289
    • Ross, A.-L.1
  • 226
    • 4544251295 scopus 로고    scopus 로고
    • Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol η and REV1 protein
    • Tissier A., Kannouche P., Reck M.-P., Lehmann A.R., Fuchs R.P.P., Cordonnier A. Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol η and REV1 protein. DNA Repair 2004, 3:1503-1514.
    • (2004) DNA Repair , vol.3 , pp. 1503-1514
    • Tissier, A.1    Kannouche, P.2    Reck, M.-P.3    Lehmann, A.R.4    Fuchs, R.P.P.5    Cordonnier, A.6
  • 227
    • 84863739595 scopus 로고    scopus 로고
    • NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase η
    • Pozhidaeva A., Pustovalova Y., D'Souza S., Bezsonova I., Walker G.C., Korzhnev D.M. NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase η. Biochemistry 2012, 51:5506-5520.
    • (2012) Biochemistry , vol.51 , pp. 5506-5520
    • Pozhidaeva, A.1    Pustovalova, Y.2    D'Souza, S.3    Bezsonova, I.4    Walker, G.C.5    Korzhnev, D.M.6
  • 228
    • 34547117417 scopus 로고    scopus 로고
    • A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage
    • Wood A., Garg P., Burgers P.M.J. A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage. J. Biol. Chem. 2007, 282:20256-20263.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20256-20263
    • Wood, A.1    Garg, P.2    Burgers, P.M.J.3
  • 229
    • 84881669109 scopus 로고    scopus 로고
    • NMR mapping of PCNA interaction with translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain
    • Pustovalova Y., Maciejewski M.W., Korzhnev D.M. NMR mapping of PCNA interaction with translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain. J. Mol. Biol. 2013, 425:3091-3105.
    • (2013) J. Mol. Biol. , vol.425 , pp. 3091-3105
    • Pustovalova, Y.1    Maciejewski, M.W.2    Korzhnev, D.M.3
  • 230
    • 33746162368 scopus 로고    scopus 로고
    • REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo
    • Guo C., Sonoda E., Tang T., Parker J., Bielen A., Takeda S., Ulrich H., Friedberg E. REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo. Mol. Cell 2006, 23:265-271.
    • (2006) Mol. Cell , vol.23 , pp. 265-271
    • Guo, C.1    Sonoda, E.2    Tang, T.3    Parker, J.4    Bielen, A.5    Takeda, S.6    Ulrich, H.7    Friedberg, E.8
  • 232
    • 79451475938 scopus 로고    scopus 로고
    • Proteasomal regulation of the mutagenic translesion DNA polymerase, Saccharomyces cerevisiae Rev1
    • Wiltrout M.E., Walker G.C. Proteasomal regulation of the mutagenic translesion DNA polymerase, Saccharomyces cerevisiae Rev1. DNA Repair 2011, 10:169-175.
    • (2011) DNA Repair , vol.10 , pp. 169-175
    • Wiltrout, M.E.1    Walker, G.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.